Crystallization and preliminary x-ray diffraction studies of a psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis(484 views) Merlino A, Russo Krauss I, Castellano I, De Vendittis E, Vergara A, Sica F
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2008; 15(4): 415-418.
Keywords: Cold Adaptation, Crystallization, Iron Superoxide Dismutase, Pseudoalteromonas Haloplanktis, X-Ray, Article, Chemistry, Dimerization, Enzymology, Isolation And Purification, X Ray Crystallography,
Affiliations: *** IBB - CNR ***
Dipartimento di Chimica, Università degli Studi di Napoli 'Federico II', Via Cintia, I-80126 Napoli, Italy
Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli 'Federico II', Via Pansini 5, I-80131 Napoli, Italy
Istituto di Biostrutture e Bioimmagini, C.N.R., via Mezzocannone 16, I-80134 Napoli, Italy
Department of Chemistry, University of Naples 'Federico II', Via Cintia, I-80126 Napoli, Italy
References: Not available.
Crystallization and preliminary x-ray diffraction studies of a psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis
The Antarctic eubacterium Pseudoalteromonas haloplanktis (Ph) produces a cold-active iron superoxide dismutase (SOD). PhSOD is a homodimeric enzyme, that displays a high catalytic activity even at low temperature. Using hanging-drop vapour-diffusion technique, PhSOD has been successfully crystallized in two different crystal forms. Both crystal forms are monoclinic with space group P2(1) and diffract to 2.1 A resolution. Form I has unit-cell parameters a=45.49A b=103.63A c=50.37A beta=108.2 degrees and contains a homodimer in the asymmetric unit. Form II has unit-cell parameters a=50.48A b=103.78A c=90.25A beta=103.8 degrees and an asymmetric unit containing two PhSOD homodimers. Structure determination has been achieved using molecular replacement. The crystallographic study of this cold-adapted enzyme could contribute to the understanding of the molecular mechanisms of cold-adaptation and of the high catalytic efficiency at low temperature.
Crystallization and preliminary x-ray diffraction studies of a psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis